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Literature summary for 2.7.11.2 extracted from

  • Hucho, F.; Randall, D.D.; Roche, T.E.; Burgett, M.W.; Pelley, J.W.; Reed, L.J.
    alpha-Keto acid dehydrogenase complexes. XVII. Kinetic and regulatory properties of pyruvate dehydrogenase kinase and pyruvate dehydrogenase phosphatase from bovine kidney and heart (1972), Arch. Biochem. Biophys., 151, 328-340.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
dihydrolipoyl transacetylase
-
Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
2-oxobutyrate
-
Bos taurus
ADP competitive to ATP Bos taurus
CaCl2 no inhibition Bos taurus
additional information no inhibition by 2-oxoglutarate; no inhibition by cAMP Bos taurus
pyruvate synergism with ADP Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0006
-
[pyruvate dehydrogenase (acetyl-transferring)] pH 7.5, 30°C Bos taurus
0.0006
-
[pyruvate dehydrogenase (acetyl-transferring)] in presence of dihydrolipoyl transacetylase Bos taurus
0.02
-
ATP kidney enzyme Bos taurus
0.02
-
Mg2+ kidney enzyme Bos taurus
0.02
-
ATP pH 7.5, 30°C Bos taurus
0.02
-
Mg2+ pH 7.5, 30°C Bos taurus
0.02
-
[pyruvate dehydrogenase (acetyl-transferring)] pH 7.5, 30°C Bos taurus
0.02
-
[pyruvate dehydrogenase (acetyl-transferring)] in absence of dihydrolipoyl transacetylase Bos taurus
0.02
-
ATP pyruvate dehydrogenase complex Bos taurus
0.02
-
Mg2+ pyruvate dehydrogenase complex Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Bos taurus 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ requirement Bos taurus
Mg2+ actual substrate: MgATP2- Bos taurus
Mn2+ requirement Bos taurus
Mn2+ can replace Mg2+ to some extent Bos taurus
additional information no activation by Ca2+ Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [pyruvate dehydrogenase (lipoamide)] Bos taurus regulatory role ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
ir
ATP + [pyruvate dehydrogenase (lipoamide)] Bos taurus catalyzes inactivation through phosphorylation of pyruvate dehydrogenase complex EC 1.2.4.1 ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
ir

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Bos taurus
-
kidney
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + casein kidney enzyme, low activity Bos taurus ADP + casein phosphate
-
?
ATP + [pyruvate dehydrogenase (acetyl-transferring)]
-
Bos taurus ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate
-
?
ATP + [pyruvate dehydrogenase (lipoamide)]
-
Bos taurus ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
ir
ATP + [pyruvate dehydrogenase (lipoamide)] regulatory role Bos taurus ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
ir
ATP + [pyruvate dehydrogenase (lipoamide)] catalyzes inactivation through phosphorylation of pyruvate dehydrogenase complex EC 1.2.4.1 Bos taurus ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
ir
additional information no activity with histones of calf thymus type II-A Bos taurus ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 7.2 in presence of Mg2+ or Mn2+ Bos taurus

pH Range

pH Minimum pH Maximum Comment Organism
5.5 8.5 about 50% or 60% of maximal activity at pH 5.5 and about 65% or 50% of maximal activity at pH 8.5, in the presence of Mg2+ or Mn2+, respectively Bos taurus

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Bos taurus
additional information no activation by cAMP Bos taurus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.1
-
ADP pH 7.5, 30°C Bos taurus